Abstract
Human secretory component has seven putative sites for N-linked glycosylation. From tryptic and Glu-C digests we have isolated peptides encompassing asparagines 65, 72, 117, 168, 403, 451 and 481. Analysis by on line HPLC-electrospray mass spectrometry indicated that these residues were fully glycosylated and that the major carbohydrate moieties were far less diversified in composition than expected. Fast atom bombardment mass spectrometry performed on oligosaccharides released by peptide- N-glycosidase F treatment of fractionated and unfractionated SC digests showed the following glycan compositions: Fuc 2Hex 5HexNAc 4, Fuc 3Hex 5HexNAc 4, NeuAcFucHex 5HexNAc 4, NeuAcFuc 2Hex 5HexNAc 4, NeuAc 2Hex 5HexNAc4 and NeuAc 2FucHex 5HexNAc 4. Three of these oligosaccharides are the major carbohydrate moieties in human lactoferrin. A possible biological role of the secretory component glycans in the protection of mucosal surfaces is discussed.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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